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Factors affecting lecithinase activity and production in Clostridium welchii*

Published online by Cambridge University Press:  15 May 2009

M. Nakamura ,
Judith A. Schulze  and
W. R. Cross
M. Nakamura
Affiliation:
Department of Microbiology, University of Montana, Missoula, Montana 59801
Judith A. Schulze
Affiliation:
Department of Microbiology, University of Montana, Missoula, Montana 59801
W. R. Cross
Affiliation:
Department of Microbiology, University of Montana, Missoula, Montana 59801
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A variety of factors that affect lecithinase activity and lecithinase production by Cl. welchii were studied. The lecithinase activity was time and temperature dependent. The optimum temperature varied from 30° to 46° C. according to the strain of Cl. welchii employed. Maximum lecithinase activity was produced after 12–60 hr. There was considerable strain variation. This could easily account for the differences in the published data.

Commercial purified lecithinase was more readily destroyed by heat than the lecithinase produced by Cl. welchii in culture media. The enzyme inactivation pattern at 60° C. was similar to that at 90° C. This is not in agreement with the reports of others who found that less enzyme was inactivated at the higher temperatures.

Acid pH values completely inactivated the enzyme. However, alkaline pH values did not significantly destroy the enzyme. The lecithovitellin reaction was completely inhibited at pH values of 1–5. The optimum pH for the reaction was around pH 7–8.

The production of lecithinase was dependent upon the pH of the culture medium. One strain produced measurable lecithinase at pH values of 5·5–8·5, whereas another strain produced lecithinase only at pH values 6–5–7–5.

Lecithin stimulated the production of lecithinase in a chemically defined medium.

Type
Research Article
Information
Journal of Hygiene , Volume 67 , Issue 1 , March 1969 , pp. 153 - 162
Copyright
Copyright © Cambridge University Press 1969

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